Literature DB >> 3720946

Membrane fusion induced by influenza virus hemagglutinin requires protein bound fatty acids.

B Lambrecht, M F Schmidt.   

Abstract

The low pH-dependent fusion of lipid membranes induced by two types of the fatty acylated influenza viral hemagglutinin has been studied by use of an energy transfer assay. When protein bound fatty acids were released from the hemagglutinin by hydroxylamine treatment viral fusion activity was inhibited. The extent of fusion inhibition correlates with the amount of fatty acids cleaved from the hemagglutinin. Virosomes prepared from fowl plague virus containing fatty acid free hemagglutinin showed a much lower fusion activity than control virosomes containing fatty acylated hemagglutinin. The hydroxylamine treatment applied has no detectable effects on the virus other than fatty acid release from its spike glycoproteins. These results support our previous hypothesis that protein bound fatty acids are involved in the induction of membrane fusion by the influenza hemagglutinin.

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Year:  1986        PMID: 3720946     DOI: 10.1016/0014-5793(86)80662-7

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  10 in total

Review 1.  Interaction of the cytoskeleton with the plasma membrane.

Authors:  V Niggli; M M Burger
Journal:  J Membr Biol       Date:  1987       Impact factor: 1.843

2.  Hapivirins and diprovirins: novel θ-defensin analogs with potent activity against influenza A virus.

Authors:  Mona Doss; Piotr Ruchala; Tesfaldet Tecle; Donald Gantz; Anamika Verma; Alex Hartshorn; Erika C Crouch; Hai Luong; Ewa D Micewicz; Robert I Lehrer; Kevan L Hartshorn
Journal:  J Immunol       Date:  2012-02-15       Impact factor: 5.422

Review 3.  N-myristoyltransferase.

Authors:  R V Rajala; R S Datla; T N Moyana; R Kakkar; S A Carlsen; R K Sharma
Journal:  Mol Cell Biochem       Date:  2000-01       Impact factor: 3.396

4.  Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF).

Authors:  A Haas; W Wickner
Journal:  EMBO J       Date:  1996-07-01       Impact factor: 11.598

5.  Palmitoylation of the 25-kDa synaptosomal protein (SNAP-25) in vitro occurs in the absence of an enzyme, but is stimulated by binding to syntaxin.

Authors:  M Veit
Journal:  Biochem J       Date:  2000-01-01       Impact factor: 3.857

6.  Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin.

Authors:  M Veit; E Kretzschmar; K Kuroda; W Garten; M F Schmidt; H D Klenk; R Rott
Journal:  J Virol       Date:  1991-05       Impact factor: 5.103

7.  Fatty acid acylation at the single cysteine residue in the cytoplasmic domain of the glycoprotein of vesicular-stomatitis virus.

Authors:  D Mack; J Kruppa
Journal:  Biochem J       Date:  1988-12-15       Impact factor: 3.857

8.  Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion.

Authors:  C W Naeve; D Williams
Journal:  EMBO J       Date:  1990-12       Impact factor: 11.598

Review 9.  Fatty acylation of proteins.

Authors:  M F Schmidt
Journal:  Biochim Biophys Acta       Date:  1989-12-06

Review 10.  Virus entry into animal cells.

Authors:  M Marsh; A Helenius
Journal:  Adv Virus Res       Date:  1989       Impact factor: 9.937

  10 in total

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